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class=\u0022pane-content\u0022\u003E\n \u003Cdiv class=\u0022elements-frag-data highwire-markup\u0022 id=\u0022fig-data\u0022\u003E\u003Cdiv id=\u0022fig-data-figures\u0022 class=\u0022group frag-figure\u0022\u003E\u003Cdiv class=\u0022fig-data-title-jump clearfix\u0022\u003E\u003Ch3 class=\u0022fig-data-group-title\u0022\u003EFigures\u003C\/h3\u003E\u003Cdiv class=\u0022fig-data-jump-links\u0022\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cdiv class=\u0022item-list\u0022\u003E\u003Cul class=\u0022fig-data-list clearfix\u0022 id=\u0022fragments-fig\u0022\u003E\u003Cli class=\u0022first\u0022\u003E\u003Cdiv class=\u0022element-fig-data clearfix figure-caption\u0022\u003E\u003Cdiv class=\u0022highwire-markup\u0022\u003E\u003Cdiv xmlns=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022 id=\u0022content-block-markup\u0022 xmlns:xhtml=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022\u003E\u003Cdiv class=\u0022fig-expansion \u0022 id=\u0022F1\u0022\u003E\u003Cspan class=\u0022highwire-journal-article-marker-start\u0022\u003E\u003C\/span\u003E\u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F1.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Sketch of the Golgi apparatus as a polarized stack of connected cisternae exchanging material. (A) Proteins synthesized in the ER go through the ER-Golgi intermediate compartment (ERGIC) before entering the Golgi through its cis face. After biochemical maturation and sorting, they exit the Golgi through the trans face to join the trans-Golgi network (TGN). (B) Relevant transport processes, including cisternal progression (translation), diffusion through connecting membrane tubules, vesicular transport, and exit. (C) Spatiotemporal evolution of an initially narrow protein distribution (as produced by a pulse of secretion from the ER); pure convection produces a uniform translation of the peak (dashed line), diffusion broadens the peak, and exit exponentially decreases the protein content.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Sketch of the Golgi apparatus as a polarized stack of connected cisternae exchanging material. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) Proteins synthesized in the ER go through the ER-Golgi intermediate compartment (ERGIC) before entering the Golgi through its \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; face. After biochemical maturation and sorting, they exit the Golgi through the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; face to join the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt;-Golgi network (TGN). (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Relevant transport processes, including cisternal progression (translation), diffusion through connecting membrane tubules, vesicular transport, and exit. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Spatiotemporal evolution of an initially narrow protein distribution (as produced by a pulse of secretion from the ER); pure convection produces a uniform translation of the peak (dashed line), diffusion broadens the peak, and exit exponentially decreases the protein content.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 1.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F1.medium.gif\u0022 width=\u0022440\u0022 height=\u0022215\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 1.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F1.medium.gif\u0022 width=\u0022440\u0022 height=\u0022215\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F1.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 1.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F1.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456371\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E\u003Cdiv class=\u0022fig-caption\u0022 xmlns:xhtml=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022\u003E\u003Cspan class=\u0022fig-label\u0022\u003EFig. 1.\u003C\/span\u003E \u003Cp id=\u0022p-7\u0022\u003ESketch of the Golgi apparatus as a polarized stack of connected cisternae exchanging material. (\u003Cem\u003EA\u003C\/em\u003E) Proteins synthesized in the ER go through the ER-Golgi intermediate compartment (ERGIC) before entering the Golgi through its \u003Cem\u003Ecis\u003C\/em\u003E face. After biochemical maturation and sorting, they exit the Golgi through the \u003Cem\u003Etrans\u003C\/em\u003E face to join the \u003Cem\u003Etrans\u003C\/em\u003E-Golgi network (TGN). (\u003Cem\u003EB\u003C\/em\u003E) Relevant transport processes, including cisternal progression (translation), diffusion through connecting membrane tubules, vesicular transport, and exit. (\u003Cem\u003EC\u003C\/em\u003E) Spatiotemporal evolution of an initially narrow protein distribution (as produced by a pulse of secretion from the ER); pure convection produces a uniform translation of the peak (dashed line), diffusion broadens the peak, and exit exponentially decreases the protein content.\u003C\/p\u003E\u003Cdiv class=\u0022sb-div caption-clear\u0022\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cspan class=\u0022highwire-journal-article-marker-end\u0022\u003E\u003C\/span\u003E\u003C\/div\u003E\u003Cspan id=\u0022related-urls\u0022\u003E\u003C\/span\u003E\u003C\/div\u003E\u003C\/div\u003E\u003C\/div\u003E\u003C\/li\u003E\n\u003Cli\u003E\u003Cdiv class=\u0022element-fig-data clearfix figure-caption\u0022\u003E\u003Cdiv class=\u0022highwire-markup\u0022\u003E\u003Cdiv xmlns=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022 id=\u0022content-block-markup\u0022 xmlns:xhtml=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022\u003E\u003Cdiv class=\u0022fig-expansion \u0022 id=\u0022F2\u0022\u003E\u003Cspan class=\u0022highwire-journal-article-marker-start\u0022\u003E\u003C\/span\u003E\u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. 3. (A and B) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (A) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (B) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (C and D) EM assays. (C) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as r. (D) Evolution of the concentration of procollagen aggregates in the cis (black) and trans (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in SI Appendix.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. \u0026lt;strong\u0026gt;3\u0026lt;\/strong\u0026gt;. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) EM assays. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as \u0026lt;em\u0026gt;r\u0026lt;\/em\u0026gt;. (\u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) Evolution of the concentration of procollagen aggregates in the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; (black) and \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in \u0026lt;em\u0026gt;SI Appendix\u0026lt;\/em\u0026gt;.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 2.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456348\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E\u003Cdiv class=\u0022fig-caption\u0022 xmlns:xhtml=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022\u003E\u003Cspan class=\u0022fig-label\u0022\u003EFig. 2.\u003C\/span\u003E \u003Cp id=\u0022p-19\u0022\u003EQuantitative analysis of data from different experimental protocols using a numerical solution of \u003Cspan id=\u0022xref-disp-formula-3-7\u0022 class=\u0022xref-disp-formula\u0022\u003EEq. \u003Cstrong\u003E3\u003C\/strong\u003E\u003C\/span\u003E. (\u003Cem\u003EA\u003C\/em\u003E and \u003Cem\u003EB\u003C\/em\u003E) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (\u003Cem\u003EA\u003C\/em\u003E) a steady influx, abruptly stopped at \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. 3. (A and B) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (A) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (B) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (C and D) EM assays. (C) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as r. (D) Evolution of the concentration of procollagen aggregates in the cis (black) and trans (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in SI Appendix.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. \u0026lt;strong\u0026gt;3\u0026lt;\/strong\u0026gt;. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) EM assays. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as \u0026lt;em\u0026gt;r\u0026lt;\/em\u0026gt;. (\u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) Evolution of the concentration of procollagen aggregates in the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; (black) and \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in \u0026lt;em\u0026gt;SI Appendix\u0026lt;\/em\u0026gt;.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 2.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456348\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E, of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (\u003Cem\u003EB\u003C\/em\u003E) a short influx, starting at \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. 3. (A and B) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (A) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (B) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (C and D) EM assays. (C) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as r. (D) Evolution of the concentration of procollagen aggregates in the cis (black) and trans (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in SI Appendix.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. \u0026lt;strong\u0026gt;3\u0026lt;\/strong\u0026gt;. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) EM assays. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as \u0026lt;em\u0026gt;r\u0026lt;\/em\u0026gt;. (\u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) Evolution of the concentration of procollagen aggregates in the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; (black) and \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in \u0026lt;em\u0026gt;SI Appendix\u0026lt;\/em\u0026gt;.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 2.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456348\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E and stopping at \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. 3. (A and B) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (A) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (B) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (C and D) EM assays. (C) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as r. (D) Evolution of the concentration of procollagen aggregates in the cis (black) and trans (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in SI Appendix.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. \u0026lt;strong\u0026gt;3\u0026lt;\/strong\u0026gt;. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) EM assays. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as \u0026lt;em\u0026gt;r\u0026lt;\/em\u0026gt;. (\u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) Evolution of the concentration of procollagen aggregates in the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; (black) and \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in \u0026lt;em\u0026gt;SI Appendix\u0026lt;\/em\u0026gt;.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 2.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456348\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E, of VSVG (\u003Cspan id=\u0022xref-ref-10-5\u0022 class=\u0022xref-bibr\u0022\u003E10\u003C\/span\u003E). \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. 3. (A and B) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (A) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (B) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (C and D) EM assays. (C) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as r. (D) Evolution of the concentration of procollagen aggregates in the cis (black) and trans (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in SI Appendix.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. \u0026lt;strong\u0026gt;3\u0026lt;\/strong\u0026gt;. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) EM assays. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as \u0026lt;em\u0026gt;r\u0026lt;\/em\u0026gt;. (\u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) Evolution of the concentration of procollagen aggregates in the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; (black) and \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in \u0026lt;em\u0026gt;SI Appendix\u0026lt;\/em\u0026gt;.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 2.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456348\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E was set to zero in the fits because it does not influence the early relaxation. (\u003Cem\u003EC\u003C\/em\u003E and \u003Cem\u003ED\u003C\/em\u003E) EM assays. (\u003Cem\u003EC\u003C\/em\u003E) Pulse-chase experiment for VSVG (\u003Cspan id=\u0022xref-ref-13-1\u0022 class=\u0022xref-bibr\u0022\u003E13\u003C\/span\u003E). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. 3. (A and B) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (A) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (B) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (C and D) EM assays. (C) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as r. (D) Evolution of the concentration of procollagen aggregates in the cis (black) and trans (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in SI Appendix.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. \u0026lt;strong\u0026gt;3\u0026lt;\/strong\u0026gt;. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) EM assays. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as \u0026lt;em\u0026gt;r\u0026lt;\/em\u0026gt;. (\u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) Evolution of the concentration of procollagen aggregates in the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; (black) and \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in \u0026lt;em\u0026gt;SI Appendix\u0026lt;\/em\u0026gt;.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 2.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456348\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E. \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. 3. (A and B) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (A) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (B) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (C and D) EM assays. (C) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as r. (D) Evolution of the concentration of procollagen aggregates in the cis (black) and trans (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in SI Appendix.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Quantitative analysis of data from different experimental protocols using a numerical solution of Eq. \u0026lt;strong\u0026gt;3\u0026lt;\/strong\u0026gt;. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Optical microscopy assays. A whole Golgi FRAP experiment probing the exit of tagged proteins from the Golgi following (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) a steady influx, abruptly stopped at , of a small transmembrane protein (VSVG) and a large soluble protein aggregate (procollagen), and (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) a short influx, starting at and stopping at , of VSVG (10). was set to zero in the fits because it does not influence the early relaxation. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt; and \u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) EM assays. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment for VSVG (13). Setting either convection (gray curve) or diffusion (dashed curve) to zero cannot reproduce the data. Fits are constrained so that the total protein concentration matches the data at . was set to zero because it has the same effect as \u0026lt;em\u0026gt;r\u0026lt;\/em\u0026gt;. (\u0026lt;em\u0026gt;D\u0026lt;\/em\u0026gt;) Evolution of the concentration of procollagen aggregates in the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; (black) and \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (9). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in \u0026lt;em\u0026gt;SI Appendix\u0026lt;\/em\u0026gt;.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 2.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.medium.gif\u0022 width=\u0022440\u0022 height=\u0022277\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 2.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F2.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456348\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E was set to zero because it has the same effect as \u003Cem\u003Er\u003C\/em\u003E. (\u003Cem\u003ED\u003C\/em\u003E) Evolution of the concentration of procollagen aggregates in the \u003Cem\u003Ecis\u003C\/em\u003E (black) and \u003Cem\u003Etrans\u003C\/em\u003E (gray) face of the Golgi upon sudden blockage of ER secretion (exiting wave experiment) (\u003Cspan id=\u0022xref-ref-9-2\u0022 class=\u0022xref-bibr\u0022\u003E9\u003C\/span\u003E). Data are in percentage of the concentration in normal conditions (steady ER secretion), and are not sensitive to exit rate. More information on the fitting procedure and experimental uncertainty is given in \u003Ca href=\u0022http:\/\/www.pnas.org\/lookup\/suppl\/doi:10.1073\/pnas.1303358110\/-\/DCSupplemental\/sapp.pdf\u0022 class=\u0022in-nw\u0022\u003E\u003Cem\u003ESI Appendix\u003C\/em\u003E\u003C\/a\u003E.\u003C\/p\u003E\u003Cdiv class=\u0022sb-div caption-clear\u0022\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cspan class=\u0022highwire-journal-article-marker-end\u0022\u003E\u003C\/span\u003E\u003C\/div\u003E\u003Cspan id=\u0022related-urls\u0022\u003E\u003C\/span\u003E\u003C\/div\u003E\u003C\/div\u003E\u003C\/div\u003E\u003C\/li\u003E\n\u003Cli\u003E\u003Cdiv class=\u0022element-fig-data clearfix figure-caption\u0022\u003E\u003Cdiv class=\u0022highwire-markup\u0022\u003E\u003Cdiv xmlns=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022 id=\u0022content-block-markup\u0022 xmlns:xhtml=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022\u003E\u003Cdiv class=\u0022fig-expansion \u0022 id=\u0022F3\u0022\u003E\u003Cspan class=\u0022highwire-journal-article-marker-start\u0022\u003E\u003C\/span\u003E\u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Localization of Golgi resident proteins. (A) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (B) Local variation of the transport rates k and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (C) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the cis face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the trans face and promotes protein exit.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Localization of Golgi resident proteins. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Local variation of the transport rates \u0026lt;em\u0026gt;k\u0026lt;\/em\u0026gt; and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; face and promotes protein exit.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 3.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456461\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E\u003Cdiv class=\u0022fig-caption\u0022 xmlns:xhtml=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022\u003E\u003Cspan class=\u0022fig-label\u0022\u003EFig. 3.\u003C\/span\u003E \u003Cp id=\u0022p-27\u0022\u003ELocalization of Golgi resident proteins. (\u003Cem\u003EA\u003C\/em\u003E) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Localization of Golgi resident proteins. (A) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (B) Local variation of the transport rates k and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (C) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the cis face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the trans face and promotes protein exit.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Localization of Golgi resident proteins. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Local variation of the transport rates \u0026lt;em\u0026gt;k\u0026lt;\/em\u0026gt; and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; face and promotes protein exit.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 3.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456461\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E, \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Localization of Golgi resident proteins. (A) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (B) Local variation of the transport rates k and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (C) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the cis face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the trans face and promotes protein exit.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Localization of Golgi resident proteins. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Local variation of the transport rates \u0026lt;em\u0026gt;k\u0026lt;\/em\u0026gt; and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; face and promotes protein exit.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 3.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456461\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E, gray curve) and for a recycling 10 times faster (black curve). (\u003Cem\u003EB\u003C\/em\u003E) Local variation of the transport rates \u003Cem\u003Ek\u003C\/em\u003E and \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Localization of Golgi resident proteins. (A) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (B) Local variation of the transport rates k and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (C) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the cis face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the trans face and promotes protein exit.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Localization of Golgi resident proteins. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Local variation of the transport rates \u0026lt;em\u0026gt;k\u0026lt;\/em\u0026gt; and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; face and promotes protein exit.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 3.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456461\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E can be converted into energy landscapes \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Localization of Golgi resident proteins. (A) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (B) Local variation of the transport rates k and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (C) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the cis face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the trans face and promotes protein exit.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Localization of Golgi resident proteins. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Local variation of the transport rates \u0026lt;em\u0026gt;k\u0026lt;\/em\u0026gt; and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; face and promotes protein exit.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 3.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456461\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Localization of Golgi resident proteins. (A) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (B) Local variation of the transport rates k and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (C) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the cis face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the trans face and promotes protein exit.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Localization of Golgi resident proteins. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Local variation of the transport rates \u0026lt;em\u0026gt;k\u0026lt;\/em\u0026gt; and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; face and promotes protein exit.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 3.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456461\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E and the corresponding rates. The steady-state distribution shows a peak where the net velocity \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Localization of Golgi resident proteins. (A) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (B) Local variation of the transport rates k and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (C) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the cis face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the trans face and promotes protein exit.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Localization of Golgi resident proteins. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Local variation of the transport rates \u0026lt;em\u0026gt;k\u0026lt;\/em\u0026gt; and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; face and promotes protein exit.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 3.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456461\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E vanishes. (\u003Cem\u003EC\u003C\/em\u003E) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the \u003Cem\u003Ecis\u003C\/em\u003E face at \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Localization of Golgi resident proteins. (A) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (B) Local variation of the transport rates k and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (C) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the cis face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the trans face and promotes protein exit.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Localization of Golgi resident proteins. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Local variation of the transport rates \u0026lt;em\u0026gt;k\u0026lt;\/em\u0026gt; and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; face and promotes protein exit.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 3.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456461\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E, and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger \u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Localization of Golgi resident proteins. (A) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (B) Local variation of the transport rates k and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (C) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the cis face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the trans face and promotes protein exit.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;\u0026lt;div xmlns=\u0026quot;http:\/\/www.w3.org\/1999\/xhtml\u0026quot;\u0026gt;Localization of Golgi resident proteins. (\u0026lt;em\u0026gt;A\u0026lt;\/em\u0026gt;) Fast recycling of proteins imported at specific Golgi location leads to a peaked protein distribution around the import location. The steady-state distribution profile is shown for parameter values corresponding to VSVG (not a resident protein, , , gray curve) and for a recycling 10 times faster (black curve). (\u0026lt;em\u0026gt;B\u0026lt;\/em\u0026gt;) Local variation of the transport rates \u0026lt;em\u0026gt;k\u0026lt;\/em\u0026gt; and can be converted into energy landscapes and related to physical mechanisms, such as hydrophobic mismatch. The example shows a quadratic landscape and the corresponding rates. The steady-state distribution shows a peak where the net velocity vanishes. (\u0026lt;em\u0026gt;C\u0026lt;\/em\u0026gt;) Pulse-chase experiment on resident proteins in a quadratic energy landscape, showing the evolution of a protein distribution initially localized at the \u0026lt;em\u0026gt;cis\u0026lt;\/em\u0026gt; face at , and the variation of the total protein content with time. Variation of the progression velocity strongly influences the protein distribution and lifetime in the Golgi. Larger (black curve) displaces the peaks toward the \u0026lt;em\u0026gt;trans\u0026lt;\/em\u0026gt; face and promotes protein exit.\u0026lt;\/div\u0026gt;\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 3.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.medium.gif\u0022 width=\u0022440\u0022 height=\u0022179\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 3.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F3.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456461\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E (black curve) displaces the peaks toward the \u003Cem\u003Etrans\u003C\/em\u003E face and promotes protein exit.\u003C\/p\u003E\u003Cdiv class=\u0022sb-div caption-clear\u0022\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cspan class=\u0022highwire-journal-article-marker-end\u0022\u003E\u003C\/span\u003E\u003C\/div\u003E\u003Cspan id=\u0022related-urls\u0022\u003E\u003C\/span\u003E\u003C\/div\u003E\u003C\/div\u003E\u003C\/div\u003E\u003C\/li\u003E\n\u003Cli class=\u0022last\u0022\u003E\u003Cdiv class=\u0022element-fig-data clearfix figure-caption\u0022\u003E\u003Cdiv class=\u0022highwire-markup\u0022\u003E\u003Cdiv xmlns=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022 id=\u0022content-block-markup\u0022 xmlns:xhtml=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022\u003E\u003Cdiv class=\u0022fig-expansion \u0022 id=\u0022F4\u0022\u003E\u003Cspan class=\u0022highwire-journal-article-marker-start\u0022\u003E\u003C\/span\u003E\u003Cdiv class=\u0022highwire-figure\u0022\u003E\u003Cdiv class=\u0022fig-inline-img-wrapper\u0022\u003E\u003Cdiv class=\u0022fig-inline-img\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F4.large.jpg?width=800\u0026amp;height=600\u0026amp;carousel=1\u0022 title=\u0022Given the evidence for intercisternal exchange during the transit of large protein complexes through the mammalian Golgi apparatus (procollagen is exchanged on average 6 times during its journey according to our analysis), we propose that PMCs could be involved in intercisternal exchange, possibly triggered by distensions in procollagen-containing cisternae. The sketch presents a snapshot of a dynamic process, showing a PMC being exchanged between two cisternae: according to our analysis, a procollagen complex is exchanged an average of six times between cisternae during its journey through the Golgi (\u0026#x223C;20 min). This may not lead to a net progression along the stack, and does not invalidate cisterna progression as the main cause for anterograde protein transport.\u0022 class=\u0022highwire-fragment fragment-images colorbox-load\u0022 rel=\u0022gallery-fragment-images-1356842089\u0022 data-figure-caption=\u0022\u0026lt;div class=\u0026quot;highwire-markup\u0026quot;\u0026gt;Given the evidence for intercisternal exchange during the transit of large protein complexes through the mammalian Golgi apparatus (procollagen is exchanged on average 6 times during its journey according to our analysis), we propose that PMCs could be involved in intercisternal exchange, possibly triggered by distensions in procollagen-containing cisternae. The sketch presents a snapshot of a dynamic process, showing a PMC being exchanged between two cisternae: according to our analysis, a procollagen complex is exchanged an average of six times between cisternae during its journey through the Golgi (\u0026#x223C;20 min). This may not lead to a net progression along the stack, and does not invalidate cisterna progression as the main cause for anterograde protein transport.\u0026lt;\/div\u0026gt;\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cspan class=\u0022hw-responsive-img\u0022\u003E\u003Cimg class=\u0022highwire-fragment fragment-image lazyload\u0022 alt=\u0022Fig. 4.\u0022 src=\u0022data:image\/gif;base64,R0lGODlhAQABAIAAAAAAAP\/\/\/yH5BAEAAAAALAAAAAABAAEAAAIBRAA7\u0022 data-src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F4.medium.gif\u0022 width=\u0022436\u0022 height=\u0022440\u0022\/\u003E\u003Cnoscript\u003E\u003Cimg class=\u0022highwire-fragment fragment-image\u0022 alt=\u0022Fig. 4.\u0022 src=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F4.medium.gif\u0022 width=\u0022436\u0022 height=\u0022440\u0022\/\u003E\u003C\/noscript\u003E\u003C\/span\u003E\u003C\/a\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cul class=\u0022highwire-figure-links inline\u0022\u003E\u003Cli class=\u0022download-fig first\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F4.large.jpg?download=true\u0022 class=\u0022highwire-figure-link highwire-figure-link-download\u0022 title=\u0022Download Fig. 4.\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload figure\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022new-tab\u0022\u003E\u003Ca href=\u0022https:\/\/www.pnas.org\/content\/pnas\/110\/39\/15692\/F4.large.jpg\u0022 class=\u0022highwire-figure-link highwire-figure-link-newtab\u0022 target=\u0022_blank\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EOpen in new tab\u003C\/a\u003E\u003C\/li\u003E\n\u003Cli class=\u0022download-ppt last\u0022\u003E\u003Ca href=\u0022\/highwire\/powerpoint\/456363\u0022 class=\u0022highwire-figure-link highwire-figure-link-ppt\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload powerpoint\u003C\/a\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E\u003Cdiv class=\u0022fig-caption\u0022 xmlns:xhtml=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022\u003E\u003Cspan class=\u0022fig-label\u0022\u003EFig. 4.\u003C\/span\u003E \u003Cp id=\u0022p-34\u0022\u003EGiven the evidence for intercisternal exchange during the transit of large protein complexes through the mammalian Golgi apparatus (procollagen is exchanged on average 6 times during its journey according to our analysis), we propose that PMCs could be involved in intercisternal exchange, possibly triggered by distensions in procollagen-containing cisternae. The sketch presents a snapshot of a dynamic process, showing a PMC being exchanged between two cisternae: according to our analysis, a procollagen complex is exchanged an average of six times between cisternae during its journey through the Golgi (\u223c20 min). This may not lead to a net progression along the stack, and does not invalidate cisterna progression as the main cause for anterograde protein transport.\u003C\/p\u003E\u003Cdiv class=\u0022sb-div caption-clear\u0022\u003E\u003C\/div\u003E\u003C\/div\u003E\u003Cspan class=\u0022highwire-journal-article-marker-end\u0022\u003E\u003C\/span\u003E\u003C\/div\u003E\u003Cspan id=\u0022related-urls\u0022\u003E\u003C\/span\u003E\u003C\/div\u003E\u003C\/div\u003E\u003C\/div\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E\u003C\/div\u003E\u003C\/div\u003E \u003C\/div\u003E\n\n \n \u003C\/div\u003E\n\u003Cdiv class=\u0022panel-separator\u0022\u003E\u003C\/div\u003E\u003Cdiv class=\u0022panel-pane pane-panels-mini pane-jnl-pnas-tab-supp\u0022 \u003E\n \n \n \n \u003Cdiv class=\u0022pane-content\u0022\u003E\n \u003Cdiv class=\u0022panel-display panel-1col clearfix\u0022 id=\u0022mini-panel-jnl_pnas_tab_supp\u0022\u003E\n \u003Cdiv class=\u0022panel-panel panel-col\u0022\u003E\n \u003Cdiv\u003E\u003Cdiv class=\u0022panel-pane pane-highwire-article-data-supp\u0022 \u003E\n \n \u003Ch2 class=\u0022pane-title\u0022\u003E\u003Cspan class=\u0022pane-title-text\u0022\u003EData supplements\u003C\/span\u003E\u003C\/h2\u003E\n \n \n \u003Cdiv class=\u0022pane-content\u0022\u003E\n \u003Cdiv class=\u0022item-list\u0022\u003E\u003Cul\u003E\u003Cli class=\u0022first last\u0022\u003E\u003Cdiv class=\u0022highwire-markup\u0022\u003E\u003Cdiv xmlns=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022 id=\u0022content-block\u0022 xmlns:xhtml=\u0022http:\/\/www.w3.org\/1999\/xhtml\u0022\u003E\u003Cdiv\u003E\u003Cspan class=\u0022highwire-journal-article-marker-start\u0022\u003E\u003C\/span\u003E\u003Cdiv class=\u0022auto-clean\u0022\u003E\u003Cspan style=\u0022font-family: Verdana,Arial,Helvetica,sans-serif; font-size: 83.33%\u0022\u003E\n \n \u003Ch2\u003ESupporting Information\u003C\/h2\u003E\n \u003Cp\u003E\u003Cstrong\u003EFiles in this Data Supplement:\u003C\/strong\u003E\u003C\/p\u003E\n \u003Cul\u003E\u003Cli\u003E\u003Ca href=\u0022\/highwire\/filestream\/613740\/field_highwire_adjunct_files\/0\/sapp.pdf\u0022 class=\u0022rewritten\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003EDownload Appendix (PDF)\u003C\/a\u003E \n \t\t\n \n \u003C\/li\u003E\u003C\/ul\u003E\n \u003C\/span\u003E\n \n \u003C\/div\u003E\u003Cspan class=\u0022highwire-journal-article-marker-end\u0022\u003E\u003C\/span\u003E\u003C\/div\u003E\u003Cspan id=\u0022related-urls\u0022\u003E\u003C\/span\u003E\u003C\/div\u003E\u003C\/div\u003E\u003C\/li\u003E\n\u003C\/ul\u003E\u003C\/div\u003E \u003C\/div\u003E\n\n \n \u003C\/div\u003E\n\u003C\/div\u003E\n \u003C\/div\u003E\n\u003C\/div\u003E\n \u003C\/div\u003E\n\n \n \u003C\/div\u003E\n\u003Cdiv class=\u0022panel-separator\u0022\u003E\u003C\/div\u003E\u003Cdiv class=\u0022panel-pane pane-earthchem\u0022 \u003E\n \n \n \n \u003Cdiv class=\u0022pane-content\u0022\u003E\n \u003Ca href=\u0022http:\/\/ecp.iedadata.org\/doidata\/10.1073\/pnas.1303358110\u0022 class=\u0022\u0022 data-icon-position=\u0022\u0022 data-hide-link-title=\u00220\u0022\u003E\u003Cimg src=\u0022http:\/\/ecp.iedadata.org\/doibanner\/10.1073\/pnas.1303358110\u0022 alt=\u0022\u0022 \/\u003E\u003C\/a\u003E \u003C\/div\u003E\n\n \n \u003C\/div\u003E\n\u003C\/div\u003E\n \u003C\/div\u003E\n\u003C\/div\u003E\n\u003C\/div\u003E\u003Cscript type=\u0022text\/javascript\u0022 src=\u0022https:\/\/www.pnas.org\/sites\/default\/files\/js\/js_hZg96SP9gBcOluDp2mGc57d8sP8uJ7g8P_JYsCISOgQ.js\u0022\u003E\u003C\/script\u003E\n\u003C\/body\u003E\u003C\/html\u003E"}